phosphonoacetic acid has been researched along with glutamic acid in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 3 (100.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Kantrowitz, ER; Middleton, SA; Tauc, P; Vachette, P | 1 |
| Kantrowitz, ER; Keiser, RT; Tauc, P; Vachette, P | 1 |
| Baker, DP; DeSena, E; Kantrowitz, ER; Stebbins, JW | 1 |
3 other study(ies) available for phosphonoacetic acid and glutamic acid
| Article | Year |
|---|---|
Structural consequences of the replacement of Glu239 by Gln in the catalytic chain of Escherichia coli aspartate transcarbamylase.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Cytidine Triphosphate; Escherichia coli; Glutamates; Glutamic Acid; Glutamine; Phosphonoacetic Acid; Protein Engineering; Structure-Activity Relationship; X-Ray Diffraction | 1990 |
Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure.
Topics: Alanine; Allosteric Regulation; Allosteric Site; Aspartate Carbamoyltransferase; Aspartic Acid; Enzyme Activation; Enzyme Stability; Escherichia coli; Glutamic Acid; Kinetics; Nucleotides; Phosphonoacetic Acid; Point Mutation; Protein Conformation; Scattering, Radiation; Succinates; Succinic Acid; X-Rays | 1994 |
Glutamic acid 86 is important for positioning the 80's loop and arginine 54 at the active site of Escherichia coli aspartate transcarbamoylase and for the structural stabilization of the C1-C2 interface.
Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Enzyme Stability; Escherichia coli; Glutamic Acid; Kinetics; Mutagenesis, Site-Directed; Phosphonoacetic Acid; Structure-Activity Relationship | 1994 |